ID A0A166LHZ2_9AGAM Unreviewed; 682 AA.
AC A0A166LHZ2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=PENSPDRAFT_747452 {ECO:0000313|EMBL:KZV76900.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76900.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV76900.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV76900.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV424462; KZV76900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166LHZ2; -.
DR STRING; 1314672.A0A166LHZ2; -.
DR InParanoid; A0A166LHZ2; -.
DR OrthoDB; 2052724at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 353..507
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 682 AA; 72939 MW; 13E9AC0EF900513F CRC64;
MSQYTFGLNP FVVVPAAGTY NNVPQVPVIV PSPARFGALP FVWHIDVLLC VLFGIFVLST
LPRAVARYTA HGELFAGLYL RRGKPTNGAR GAAIATVPAA GHAMPKTPVP EAAMMMHDGA
TVDDEGTMRL DAADAGLNEP AMPASSTTAS HAALLNYAVV DSDNGARQAV NPPAHISSYL
ALTHPVISYV ANFPVAAGLP FKHFAVLLIY FGILLYVGVR GTSPFTDPRR PVDVAISQLP
FVLAFSQKNN VLAVLSGLGY EKLNYLHRFV GRIIVLGVNL HTSYYLYRWS LDGTIYAQSR
TSFVVWGIIG TAAVDVLFLL STAYVRARAY GLFLASHIFL SGLFVVAMYI HEPVTLPYFV
TAFVLYGADH IFRAMRTRIV TVDLTAAPLL NGGSTIVSAP SLTTGWRAGQ HVRMRIIPAR
GPRWLAVSWT WFAARFRARP FTISTRPGSS RGLELIVKKE GRSTQALFAR ATKDCPGSDG
DPEKQCTGAC VKATVLLEGP YSGPGHALPQ AFSGALLLAG GSGITHALAL LDALAEAHAN
GRSSCRVVDL VWATPDIASC VPLLPRFREL LAPRPSPHGS FMVRVSIHYT RVSSGAMKAL
NPAELPAGLV LHAGRPYVRT VLADACRATA AAHPGVRPRG LVVSTCGPAQ ISEQAHAAVG
SIAWDHWREV GGIEIVSETF GM
//